Intragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly-213 to Asn: Functional interactions between residues in the proton transport site

Biochemical Journal

Volumn 347, Issue 3, 2000, Pages 797-805

  Kuo, Phillip H ^a   Nakamoto, Robert K ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

Author keywords

Coupling; Isokinetic analysis; Rotational catalysis; Transition state

Indexed keywords

ADENOSINE TRIPHOSPHATE; ARGININE; ASPARAGINE; GLYCINE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENTHALPY; ENTROPY; ENZYME SUBUNIT; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTON TRANSPORT; STEADY STATE;

ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; ARGININE; BINDING SITES; BIOLOGICAL TRANSPORT, ACTIVE; BLOTTING, WESTERN; CARBONYL CYANIDE M-CHLOROPHENYL HYDRAZONE; CATALYSIS; CYSTEINE; ELECTRON TRANSPORT; ESCHERICHIA COLI; GENES, SUPPRESSOR; INTRACELLULAR MEMBRANES; KINETICS; NAD; OXIDATIVE PHOSPHORYLATION; PROTEIN STRUCTURE, SECONDARY; PROTON-MOTIVE FORCE; PROTON-TRANSLOCATING ATPASES; PROTONS; SUPPRESSION, GENETIC; THERMODYNAMICS;

EID: 0034193433     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3470797     Document Type: Article

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